TYPH_RAT
ID TYPH_RAT Reviewed; 476 AA.
AC Q5FVR2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Thymidine phosphorylase;
DE Short=TP;
DE EC=2.4.2.4;
DE AltName: Full=TdRPase;
GN Name=Tymp; Synonyms=Ecgf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6 AND THR-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of thymidine. The
CC produced molecules are then utilized as carbon and energy sources or in
CC the rescue of pyrimidine bases for nucleotide synthesis (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +
CC thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.4;
CC -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC dTMP from thymine: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC089830; AAH89830.1; -; mRNA.
DR RefSeq; NP_001012122.1; NM_001012122.1.
DR AlphaFoldDB; Q5FVR2; -.
DR SMR; Q5FVR2; -.
DR STRING; 10116.ENSRNOP00000039935; -.
DR BindingDB; Q5FVR2; -.
DR ChEMBL; CHEMBL1075244; -.
DR iPTMnet; Q5FVR2; -.
DR PhosphoSitePlus; Q5FVR2; -.
DR PaxDb; Q5FVR2; -.
DR Ensembl; ENSRNOT00000040541; ENSRNOP00000039935; ENSRNOG00000032394.
DR GeneID; 315219; -.
DR KEGG; rno:315219; -.
DR CTD; 1890; -.
DR RGD; 1305756; Tymp.
DR eggNOG; ENOG502QPRY; Eukaryota.
DR GeneTree; ENSGT00390000009250; -.
DR HOGENOM; CLU_025040_0_2_1; -.
DR InParanoid; Q5FVR2; -.
DR OMA; DVWRRMI; -.
DR OrthoDB; 1462537at2759; -.
DR PhylomeDB; Q5FVR2; -.
DR TreeFam; TF332198; -.
DR Reactome; R-RNO-73614; Pyrimidine salvage.
DR Reactome; R-RNO-73621; Pyrimidine catabolism.
DR UniPathway; UPA00578; UER00638.
DR PRO; PR:Q5FVR2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000032394; Expressed in liver and 19 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
DR GO; GO:0009032; F:thymidine phosphorylase activity; ISO:RGD.
DR GO; GO:0046074; P:dTMP catabolic process; ISO:RGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; ISO:RGD.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; ISO:RGD.
DR GO; GO:1905333; P:regulation of gastric motility; ISO:RGD.
DR GO; GO:0031641; P:regulation of myelination; ISO:RGD.
DR GO; GO:0051969; P:regulation of transmission of nerve impulse; ISO:RGD.
DR Gene3D; 3.40.1030.10; -; 1.
DR Gene3D; 3.90.1170.30; -; 1.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR InterPro; IPR036566; PYNP-like_C_sf.
DR InterPro; IPR013102; PYNP_C.
DR InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
DR InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR PANTHER; PTHR10515; PTHR10515; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR Pfam; PF07831; PYNP_C; 1.
DR PIRSF; PIRSF000478; TP_PyNP; 1.
DR SMART; SM00941; PYNP_C; 1.
DR SUPFAM; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR SUPFAM; SSF54680; SSF54680; 1.
DR TIGRFAMs; TIGR02644; Y_phosphoryl; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..476
FT /note="Thymidine phosphorylase"
FT /id="PRO_0000319099"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 476 AA; 49901 MW; 1BB6068E2D94D24A CRC64;
MAAPGTPPPL APETAGADSG GGSGEHRQLP ELIRLKRNGG HLSEADIRNF VHALMDGRAQ
DTQIGAMLMA IRLQGMDLEE TSVLTQALAE SGQQLEWPKA WHQQLVDKHS TGGVGDKVSL
VLAPALAACG CKVPMISGRS LGHTGGTLDK LESIPGFSVT QSPEQMLQIL EEVGCCIVGQ
SEKLVPADGI LYAARDVTAT VDSVPLITAS ILSKKAVEGL STLVVDVKFG GAAVFPDQEK
ARELAKMLVR VGMGLGLQVA AALTAMDNPL GRNVGHTLEV EEALLCLDGA GPPDLRDLVI
RLGGAILWLS GQAETQDQGA ARVAAALDDG SALHRFQLML SAQGVDPGLA RALCSGSPTQ
RRQLLPHARK QEELLSPADG IVECVRALPL ACVLHELGAG RSRAGQPIRP GVGAELLVDV
GQWLSRGTPW LRVHLDGPAL SSQQRRTLLG ALVLSDRAPF KAPSPFAELV LPPTTP
